1wap
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(New page: 200px<br /><applet load="1wap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wap, resolution 1.8Å" /> '''TRP RNA-BINDING ATTEN...)
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Revision as of 03:09, 21 November 2007
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TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN
Overview
The crystal structure of the trp RNA-binding attenuation protein of, Bacclius subtilis solved at 1.8 A resolution reveals a novel structural, arrangement in which the eleven subunits are stabilized through eleven, intersubunit beta-sheets to form a beta-wheel with a large central hole., The nature of the binding of L-tryptophan in clefts between adjacent, beta-sheets in the beta-wheel suggests that this binding induces, conformational changes in the flexible residues 25-33 and 49-52. It is, argued that upon binding, the messenger RNA target forms a matching circle, in which eleven U/GAG repeats are bound to the surface of the protein, ondecamer modified by the binding of L-tryptophan.
About this Structure
1WAP is a Single protein structure of sequence from Bacillus subtilis with TRP as ligand. Full crystallographic information is available from OCA.
Reference
The structure of trp RNA-binding attenuation protein., Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P, Nature. 1995 Apr 20;374(6524):693-700. PMID:7715723
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